THI7_YEAST
ID THI7_YEAST Reviewed; 598 AA.
AC Q05998; D6VYN5; P87335;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Thiamine transporter;
GN Name=THI7; Synonyms=THI10; OrderedLocusNames=YLR237W; ORFNames=L8083.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=9235906; DOI=10.1074/jbc.272.31.19165;
RA Enjo F., Nosaka K., Ogata M., Iwashima A., Nishimura H.;
RT "Isolation and characterization of a thiamin transport gene, THI10, from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:19165-19170(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Responsible for intake of thiamine.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 3120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR EMBL; U19027; AAB67405.1; -; Genomic_DNA.
DR EMBL; D55634; BAA09504.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09551.1; -; Genomic_DNA.
DR PIR; S51456; S51456.
DR RefSeq; NP_013338.1; NM_001182124.1.
DR AlphaFoldDB; Q05998; -.
DR SMR; Q05998; -.
DR BioGRID; 31504; 106.
DR DIP; DIP-4784N; -.
DR IntAct; Q05998; 3.
DR MINT; Q05998; -.
DR STRING; 4932.YLR237W; -.
DR TCDB; 2.A.39.4.1; the nucleobase:cation symporter-1 (ncs1) family.
DR iPTMnet; Q05998; -.
DR MaxQB; Q05998; -.
DR PaxDb; Q05998; -.
DR PRIDE; Q05998; -.
DR EnsemblFungi; YLR237W_mRNA; YLR237W; YLR237W.
DR GeneID; 850938; -.
DR KEGG; sce:YLR237W; -.
DR SGD; S000004227; THI7.
DR VEuPathDB; FungiDB:YLR237W; -.
DR eggNOG; KOG2466; Eukaryota.
DR GeneTree; ENSGT00940000176299; -.
DR HOGENOM; CLU_021555_3_0_1; -.
DR InParanoid; Q05998; -.
DR OMA; WPTQPWL; -.
DR BioCyc; YEAST:G3O-32346-MON; -.
DR PRO; PR:Q05998; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05998; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:1903089; F:5-amino-1-ribofuranosylimidazole-4-carboxamide transmembrane transporter activity; IGI:SGD.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IMP:SGD.
DR GO; GO:1903088; P:5-amino-1-ribofuranosylimidazole-4-carboxamide transmembrane transport; IGI:SGD.
DR GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR GO; GO:0015888; P:thiamine transport; IMP:SGD.
DR InterPro; IPR012681; NCS1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR TIGRFAMs; TIGR00800; ncs1; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..598
FT /note="Thiamine transporter"
FT /id="PRO_0000197926"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 598 AA; 66904 MW; 5160ADCAFC68A39E CRC64;
MSFGSKVSRA LRFLEIPVKD RASVSFLKNP DLQPIKSANQ TWGFWSNFAY WGVMSFSVGT
WMSASSALGV GLSYPETIGT FIVGDVLTII FTLANSCPGY DWKVGFTLAQ RFVFGIYGSA
FGIIIRILMS IVNYGSNAWV GGLCINMILD SWSHHYLHLP NTLSSKVAMT TKELIGFIIF
HVLTAFCYLM KPYHMNYILI WSCVATFFSM LGMVIYLAKQ AHGVGELFTS TKSTATGSTK
AWAWVYMISY WFGSVSPGST NQSDYSRFGS SNWAIWAGTI CALLIPTTLI PVFGVIGAST
CDKLYGEQYW MPMDIFNHWL TTNYSAGARA GAFFCGLSFV LSQMSYTISN CGFASGMDLA
GLLPKYVDIK RGALFAACVS WACLPWNFYN SSSTFLTVMS SFGVVMTPII SVMICDNFLI
RKRQYSITNA FILKGEYYFT KGVNWRAIVA WVCGMTPGLP GIAWEVNNDY FHNTGIVNFF
YGDSFFSFLI SFFVYWGLCL LFPFKITVKH DDKDYYGAFT DEEARKKGMV PYSEISEEEI
RAYTLGEGYT TGHEYRPEGS DDEIPELVKT SSENTNEFEI VHHKNNEKQS STASEKAA
